活动站点
人工酶
超分子化学
化学
组合化学
肽
酶
催化作用
DNA
纳米技术
生物化学
材料科学
分子
有机化学
作者
Siyuan Liu,Peidong Du,Hao Sun,Hai‐Yin Yu,Zhen‐Gang Wang
出处
期刊:ACS Catalysis
日期:2020-12-04
卷期号:10 (24): 14937-14958
被引量:41
标识
DOI:10.1021/acscatal.0c03753
摘要
Enzymes play vital roles in cellular functions by catalyzing biochemical reactions in high activity and selectivity, which is largely attributed to the cooperation between the exquisitely distributed functional groups at the active sites. Reconstruction of the enzymatic active sites in the artificial systems, to produce active and robust biocatalysts, has been a significant but challenging subject. Biomolecular self-assembly, typically with de novo designed peptide or DNA as the building blocks, provides an effective avenue to orient and confine reactive groups into a catalytically active configuration to mimic and even rival the catalytic performance of native enzymes. In this Review, we discuss the chemical and structural properties of DNA and peptide self-assemblies, and principles and strategies of designing active sites that show hydrolase-, peroxidase-, oxidase-, or aldolase-like activities. We focus on the relationship between and control over the structures of the artificial active sites and catalytic performances. We also highlight the synergies between the components in the formation of the active sites, as well as the applications of the artificial enzymes. In the end, we provide an outlook on the obstacles, possible solutions, and future directions, in the aspect of structural modeling, improving catalytic performances, and upgrading complexity of the active sites.
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